Chemical Antibody Mimics Inhibit Cadherin‐Mediated Cell–Cell Adhesion: A Promising Strategy for Cancer Therapy

Rangel, Paulina X. Medina; Moroni, Elena; Merlier, Franck; Gheber, Levi A.; Vago, Razi; Bui, Bernadette Tse Sum; Haupt, Karsten

doi:10.1002/ange.201910373

Cited by 26 publications

(21 citation statements)

References 53 publications

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“…When synthesized in the form of nanoparticles, 5 − 7 MIP-NPs display a close resemblance to antibodies, having a low number of binding sites per NP and a high affinity for the target analyte. Thus, MIP-NPs are ideal for functional interactions with biomolecules, opening applications in molecular diagnosis both at the cell and tissue levels, 8 for in vivo removal of toxins, 5 for interfering with metastatic proliferation, 9 , 10 for protein refolding, 11 or for acting as targeted prodrugs in contrasting the growth of cancer cells. 12 …”

Section: Introductionmentioning

confidence: 99%

Molecularly Imprinted Silk Fibroin Nanoparticles

Bossi

Bucciarelli

Maniglio

2021

ACS Appl. Mater. Interfaces

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Nanosized biomimetics prepared by the strategy of molecular imprinting, that is, the stamping of recognition sites by means of a template-assisted synthesis, are demonstrating potential as plastic antibodies in medicine, proving effective for cell imaging and targeted therapies. Most molecularly imprinted nanoparticles (MIP-NPs) are currently made of soft matter, such as polyacrylamide and derivatives. Yet, MIP-NPs biocompatibility is crucial for their effective translation into clinical uses. Here, we propose the original idea to synthesize fully biocompatible molecularly imprinted nanoparticles starting from the natural polymer silk fibroin (MIP SF-NPs), which is nontoxic and highly biocompatible. The conditions to produce MIP SF-NPs of different sizes ( d mean ∼ 50 nm; d mean ∼ 100 nm) were set using the response surface method. The stamping of a single, high affinity ( K D = 57 × 10 –9 M), and selective recognition site per silk fibroin nanoparticle was demonstrated, together with the confirmation of nontoxicity. Additionally, MIP SF-NPs were used to decorate silk microfibers and silk nanofibers, providing a general means to add entailed biofunctionalities to materials.

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Section: Introductionmentioning

confidence: 99%

Molecularly Imprinted Silk Fibroin Nanoparticles

Bossi

Bucciarelli

Maniglio

2021

ACS Appl. Mater. Interfaces

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“…There are several studies focusing on imprinting of small molecules [ 40 ], peptides [ 41 ] and proteins [ 42 , 43 ], however, there is still a great challenge about imprinting of microorganisms [ 22 ]. The three-dimensional shape, size and complex surface chemistry of the microorganisms contribute to reduce the sensitivity when using SPR for quantifying microorganisms.…”

Section: Resultsmentioning

confidence: 99%

Whole Cell Recognition of Staphylococcus aureus Using Biomimetic SPR Sensors

et al. 2021

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Over the past few decades, a significant increase in multi-drug-resistant pathogenic microorganisms has been of great concern and directed the research subject to the challenges that the distribution of resistance genes represent. Globally, high levels of multi-drug resistance represent a significant health threat and there is a growing requirement of rapid, accurate, real-time detection which plays a key role in tracking of measures for the infections caused by these bacterial strains. It is also important to reduce transfer of resistance genes to new organisms. The, World Health Organization has informed that millions of deaths have been reported each year recently. To detect the resistant organisms traditional detection approaches face limitations, therefore, newly developed technologies are needed that are suitable to be used in large-scale applications. In the present study, the aim was to design a surface plasmon resonance (SPR) sensor with micro-contact imprinted sensor chips for the detection of Staphylococcus aureus. Whole cell imprinting was performed by N-methacryloyl-L-histidine methyl ester (MAH) under UV polymerization. Sensing experiments were done within a concentration range of 1.0 × 102–2.0 × 105 CFU/mL. The recognition of S. aureus was accomplished by the involvement of microcontact imprinting and optical sensor technology with a detection limit of 1.5 × 103 CFU/mL. Selectivity of the generated sensor was evaluated through injections of competing bacterial strains. The responses for the different strains were compared to that of S. aureus. Besides, real experiments were performed with milk samples spiked with S. aureus and it was demonstrated that the prepared sensor platform was applicable for real samples.

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“…More recently, the perspective moved to therapy. Protein imprinted polymers (pMIPs) raise expectations for playing more dynamic clinical roles by acting as direct interferents amid cellular interactions, such as playing a role in preventing protein dimerization [17,18]. The stakes for succeeding with pMIP materials as therapeutics are very high.…”

Section: Reasons For Protein Imprintingmentioning

confidence: 99%

“…2C); thus, the orientation of the epitope during the imprinting process shall also be carefully considered. Template orientation control can be achieved by exploiting inhibitors, such as benzamidine, that work to directionally immobilize the template, i.e., a serineprotease enzyme via its active site [44], or more generally by coupling the epitope to a solid support in a defined direction, which is a practice that takes advantage of the classical coupling chemistries, such as carbodiimide/succinimide [25], glutaraldehyde [25], and more recently of click chemistry [17]. A further example on how to directionally immobilize an epitope lies in tagging the targeted protein with a common biochemical tag, such as the His-tag [45] or the FLAG tag [46].…”

Section: Reasons For Protein Imprintingmentioning

confidence: 99%

Molecularly imprinted polymers by epitope imprinting: a journey from molecular interactions to the available bioinformatics resources to scout for epitope templates

Pasquardini¹,

Bossi

2021

Anal Bioanal Chem

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The molecular imprinting of proteins is the process of forming biomimetics with entailed protein-recognition by means of a template-assisted synthesis. Protein-imprinted polymers (pMIPs) have been successfully employed in separations, assays, sensors, and imaging. From a technical point of view, imprinting a protein is both costly, for protein expression and purification, and challenging, for the preservation of the protein’s structural properties. In fact, the imprinting process needs to guarantee the preservation of the same protein three-dimensional conformation that later would be recognized. So far, the captivating idea to imprint just a portion of the protein, i.e., an epitope, instead of the whole, proved successful, offering reduced costs, compatibility with many synthetic conditions (solvents, pH, temperatures), and fine-tuning of the peptide sequence so to target specific physiological and functional conditions of the protein, such as post-translational modifications. Here, protein-protein interactions and the biochemical features of the epitopes are inspected, deriving lessons to prepare more effective pMIPs. Epitopes are categorized in linear or structured, immunogenic or not, located at the protein’s surface or buried in its core and the imprinting strategies are discussed. Moreover, attention is given to freely available online bioinformatics resources that might offer key tools to gain further rationale amid the selection process of suitable epitopes templates.

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Chemical Antibody Mimics Inhibit Cadherin‐Mediated Cell–Cell Adhesion: A Promising Strategy for Cancer Therapy

Cited by 26 publications

References 53 publications

Molecularly Imprinted Silk Fibroin Nanoparticles

Molecularly Imprinted Silk Fibroin Nanoparticles

Whole Cell Recognition of Staphylococcus aureus Using Biomimetic SPR Sensors

Molecularly imprinted polymers by epitope imprinting: a journey from molecular interactions to the available bioinformatics resources to scout for epitope templates

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